ArticleBiophysical journal1992
Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins.
Article in Biophysical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- COMP Is a Biomarker of Cartilage Destruction, Extracellular Matrix and Vascular Remodeling and Tissue Repair.International journal of molecular sciences · 2025Review
- Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats.Protein science : a publication of the Protein Society · 2019Article
- The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system.Nucleus (Austin, Tex.) · 2017Article
- Nesprins: from the nuclear envelope and beyond.Expert reviews in molecular medicine · 2013Review
- Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study.Journal of biomolecular NMR · 2012Article
- The crystal structures of dystrophin and utrophin spectrin repeats: implications for domain boundaries.PloS one · 2012Article
- Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.Blood · 2010Article
- Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior.PLoS computational biology · 2009Article
- A Two-amino Acid Mutation Encountered in Duchenne Muscular Dystrophy Decreases Stability of the Rod Domain 23 (R23) Spectrin-like Repeat of Dystrophin.The Journal of biological chemistry · 2009Article
- Molecular epitopes of the ankyrin-spectrin interaction.Biochemistry · 2008Article
- Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Biophysical journal · 2006Article
- Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization.BMC bioinformatics · 2003Article
- Structure of a genetically engineered molecular motor.The EMBO journal · 2001Article
- Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits.Nucleic acids research · 2000Article
- From coiled coils to small globular proteins: design of a native-like three-helix bundle.Protein science : a publication of the Protein Society · 1998Article
- Influence of network topology on the elasticity of the red blood cell membrane skeleton.Biophysical journal · 1997Article
- Myosin motors with artificial lever arms.The EMBO journal · 1996Article
- Stability of the dystrophin rod domain fold: evidence for nested repeating units.Biophysical journal · 1996Article
Corrections and comments
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Authors and funding
3 authors.
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Abstract
Members of the spectrin superfamily of proteins contain different numbers of homologous repeats arranged in tandem. Each of these consists of a three-alpha-helix motif, comprising two similarly and one oppositely directed alpha-helical segment joined by nonhelical linkers of characteristic length. The right-handed alpha-helices each display a heptad repeat in their amino acid sequences indicative of left-handed coiled-coil-like packing. We have calculated the potential number of inter-helix ionic interactions that specify the spatial arrangement of the helices in the motif in terms of both the handedness of helix connectivity (left or right) and the relative axial stagger between the three alpha-helices. All of the models examined were constrained to have optimal coiled-coil packing. For alpha-spectrin and alpha-actinin the results provide strong support for a left-handed connectivity of the three helices and axial repeat lengths of 5.05 and 6.24 nm, respectively. Furthermore, the axial staggers between homologous segments in the preferred models are identical. The insights provided into the topography of this widespread tertiary fold may prove of value to those concerned with the problem of de novo protein design.
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